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- W2034940186 endingPage "649" @default.
- W2034940186 startingPage "635" @default.
- W2034940186 abstract "The phosphorylation of proteins on tyrosine residues, initially believed to be primarily involved in cell growth and differentiation, is now recognized as having a critical role in regulating the function of mature cells. The brain exhibits one of the highest levels of tyrosine kinase activity in the adult animal and the synaptic region is particularly rich in tyrosine kinases and phosphorylated proteins. Recent studies have described the effects of tyrosine phosphorylation on the activities of a number of proteins which are potentially involved in the regulation of synaptic function. Furthermore, it is becoming apparent that tyrosine phosphorylation is involved in the modification of synaptic activity, such as occurs during depolarization, the induction of long-term potentiation or long-term depression, and ischemia. Changes in the activities of tyrosine kinases and/or protein tyrosine phosphatases which are associated with synaptic structures may result in altered tyrosine phosphorylation of proteins located at the synapse leading to both short-term and long-lasting changes in synaptic and neuronal function." @default.
- W2034940186 created "2016-06-24" @default.
- W2034940186 creator A5027841522 @default.
- W2034940186 date "1997-11-01" @default.
- W2034940186 modified "2023-10-18" @default.
- W2034940186 title "Protein tyrosine phosphorylation: Implications for synaptic function" @default.
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